Penetration of leucine and norleucine into lecithin monolayers from underlying aqueous solutions.

概要

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The surface pressure of the monolayers of dimyristoyl phosphatidylcholine(DMPC) on leucine and norleucine solutions was measured and the amounts of these amino acids which had penetrated into the DMPC monolayer were calculated by means of a successive approximation. Although the amounts of leucine and norleucine adsorbed onto the solution surface were nearly equal and were larger than that of lysine, the amount of leucine which had penetrated into the DMPC monolayer was remarkably small. That of norleucine was not so small, but was still smaller than that of lysine except for the region where the molecular area of DMPC is large. The partial molecular areas of amino acid, \barA2, and DMPC, \barA3, were calculated in each case. The value of \barA2, was the largest in the case of leucine and the smallest in the case of lysine, which means that the area occupied by lysine is smaller than that of norleucine because the interaction of ε-amino group with DMPC contracts the mixed monolayer. The change in the value of \barA3 due to the interaction with amino acid, however, was not large, which means that the change in the state of DMPC itself is not large and rather independent of the kind of amino acid.
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